Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes in COS-1 cells and in Pichia pastoris strain GS115 | Cypridina noctiluca |
Protein Variants | Comment | Organism |
---|---|---|
additional information | wild-type and mutant enzymes show similar secretion efficiencies, and thermostabilities at 25-37°C, overview | Cypridina noctiluca |
N182D | site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant enzyme behaves similar compared to the wild-type | Cypridina noctiluca |
N182D/N404D | site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows over slightly increased protein accumulation compared to the wild-type | Cypridina noctiluca |
N182D/S406A | site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows over slightly increased protein accumulation compared to the wild-type | Cypridina noctiluca |
N404D | site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant enzyme behaves similar to the wild-type | Cypridina noctiluca |
S406A | site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows increased protein accumulation compared to the wild-type | Cypridina noctiluca |
T184A | site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows increased protein accumulation compared to the wild-type | Cypridina noctiluca |
T184A/N404D | site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows over 2.5fold increased protein accumulation compared to the wild-type | Cypridina noctiluca |
T184A/S406A | site-directed mutagenesis, mutation of a residue involved in a phoshorylation site, the mutant shows over slightly increased protein accumulation compared to the wild-type | Cypridina noctiluca |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | the enzyme is secreted | Cypridina noctiluca | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cypridina noctiluca | Q75R40 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | the enzyme has two N-glycosylation sites with the consensus sequence for N-glycosylation (Asn-X-Ser/Thr). The producibility and relative specific activity are apparently reduced in Cluc mutated in the phosphorylation sites, although the thermostability and secretion efficiency are not affected. N-glycosylation modifications and the proper amino acid sequence of the N-glycan binding sites of Cluc are required for the complete protein folding to form a stable catalytic center, for the proper conformation of substrate-protein interaction residues, or for both. Defects in the glycosylation modification are not related to secretion process and stability of the protein | Cypridina noctiluca |
Subunits | Comment | Organism |
---|---|---|
? | x * 60000, mature enzyme Cluc, SDS-PAGE | Cypridina noctiluca |
Synonyms | Comment | Organism |
---|---|---|
CLuc | - |
Cypridina noctiluca |
Cypridina luciferase | - |
Cypridina noctiluca |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Cypridina noctiluca |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Cypridina noctiluca |
General Information | Comment | Organism |
---|---|---|
malfunction | Producibility and relative specific activity are apparently reduced in Cluc mutated in the phosphorylation sites, although the thermostability and secretion efficiency are not affected. Defects in the glycosylation modification are not related to secretion process and stability of the protein | Cypridina noctiluca |